ID   PRIL_THEVO              Reviewed;         327 AA.
AC   Q97BA1;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701};
GN   Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; Synonyms=priB;
GN   OrderedLocusNames=TV0556; ORFNames=TVG0544022;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Regulatory subunit of DNA primase, an RNA polymerase that
CC       catalyzes the synthesis of short RNA molecules used as primers for DNA
CC       polymerase during DNA replication. Stabilizes and modulates the
CC       activity of the small subunit, increasing the rate of DNA synthesis,
CC       and conferring RNA synthesis capability. The DNA polymerase activity
CC       may enable DNA primase to also catalyze primer extension after primer
CC       synthesis. May also play a role in DNA repair. {ECO:0000255|HAMAP-
CC       Rule:MF_00701}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00701};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00701};
CC   -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC       (PriL). {ECO:0000255|HAMAP-Rule:MF_00701}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00701}.
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DR   EMBL; BA000011; BAB59698.1; -; Genomic_DNA.
DR   RefSeq; WP_010916815.1; NC_002689.2.
DR   AlphaFoldDB; Q97BA1; -.
DR   STRING; 273116.14324771; -.
DR   DNASU; 1441073; -.
DR   EnsemblBacteria; BAB59698; BAB59698; BAB59698.
DR   GeneID; 1441073; -.
DR   KEGG; tvo:TVG0544022; -.
DR   eggNOG; arCOG03013; Archaea.
DR   HOGENOM; CLU_052778_0_0_2; -.
DR   OMA; ITRYQIK; -.
DR   OrthoDB; 29893at2157; -.
DR   PhylomeDB; Q97BA1; -.
DR   Proteomes; UP000001017; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003896; F:DNA primase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06560; PriL; 1.
DR   HAMAP; MF_00701; DNA_primase_lrg_arc; 1.
DR   InterPro; IPR007238; DNA_primase_lsu_euk/arc.
DR   InterPro; IPR023642; DNA_primase_lsu_PriL.
DR   PANTHER; PTHR10537; PTHR10537; 1.
DR   Pfam; PF04104; DNA_primase_lrg; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; DNA replication; Iron; Iron-sulfur; Metal-binding; Primosome.
FT   CHAIN           1..327
FT                   /note="DNA primase large subunit PriL"
FT                   /id="PRO_0000046790"
FT   BINDING         218
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         290
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         299
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
FT   BINDING         307
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00701"
SQ   SEQUENCE   327 AA;  37915 MW;  55A1A467BAAC1645 CRC64;
     MRFPPLLFFQ DSEAVKRIAN SVRGTKDDDA EIKDHSMRFI RNAISGDQQK EILNVDMLRY
     IAWVLVALNE NIVTARTVIR ERDAVEDALK NQQPEDIENF ADDLKINMKY NRDLERFEIG
     VFDFVKYASR VTGSQYRLSN QSVIKGIVYC QKDVAIKILR ESFVSNMFKV IDSIDQTTAS
     PVLSDQTDSI NELREFYKKS VYAKLTIGRG NTKAFPPCMK EIIRNLHEGI NVPHMGRLAI
     ASFLHKVGYT EDEIVEYFRN APDFDESITR YQIKHLSGEI SGVEYSPPKC ETMRSNHLCF
     MDDDKLCHQD WMKHPLTYYE VKSRRLG